Intrinsically disordered region of talin’s FERM domain functions as an initial PIP2 recognition site
This allows for interaction with PIP2 even in Talin’s autoinhibited form and paves the way to establish known binding surfaces.
Follow the QR code or visit https://github.com/hits-mbm-dev/paper-talin-loop for the repository of the paper draft. Or even better yet, talk to me in front of the poster!
Focal adhesions mediate the interaction of the cytoskeleton with the extracellular matrix (ECM). Talin is a central regulator and adaptorprotein of the multiprotein focal adhesion complexes and is responsible for integrin activation and force-sensing. We evaluated direct interactions of talin with the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) by means of molecular dynamics simulations. A newly published autoinhibitory structure of talin, where common PIP2 interaction sites are covered up, sparked our curiosity for a hitherto less examined loop as a potential site of first contact. We show that this unstructured loop in the F1 subdomain of the talin1 FERM domain is able to interact with PIP2 and can facilitate further interactions by serving as a flexible membrane anchor.
This project has received funding from the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement No. 101002812)
This poster was made betterposter (Aden-Buie 2022) R package and quarto (Allaire et al. 2022).